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Volumn 240, Issue 2, 1999, Pages 307-316

The Arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin

Author keywords

Arabidopsis thaliana; Chloroplast; Evolution; Redox; Thioredoxin

Indexed keywords

THIOREDOXIN;

EID: 0032735140     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(99)00448-5     Document Type: Article
Times cited : (67)

References (37)
  • 1
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner F.R., et al. The complete genome sequence of Escherichia coli K-12. Science. 277:1997;1453-1474.
    • (1997) Science , vol.277 , pp. 1453-1474
    • Blattner, F.R.1
  • 2
    • 0000765807 scopus 로고
    • Role of light in the regulation of chloroplast enzymes
    • Buchanan B.B. Role of light in the regulation of chloroplast enzymes. Ann. Rev. Plant Physiol. 31:1980;341-374.
    • (1980) Ann. Rev. Plant Physiol. , vol.31 , pp. 341-374
    • Buchanan, B.B.1
  • 4
    • 0000479431 scopus 로고
    • Isolation of plant DNA from fresh tissue
    • Doyle J.J., Doyle J.L. Isolation of plant DNA from fresh tissue. Focus. 12:1989;13-15.
    • (1989) Focus , vol.12 , pp. 13-15
    • Doyle, J.J.1    Doyle, J.L.2
  • 5
    • 0026656815 scopus 로고
    • Exhaustive matching of the entire protein sequence database
    • Gonnet G.H., Cohen M.A., Benner S.A. Exhaustive matching of the entire protein sequence database. Science. 256:1992;1443-1445.
    • (1992) Science , vol.256 , pp. 1443-1445
    • Gonnet, G.H.1    Cohen, M.A.2    Benner, S.A.3
  • 6
    • 0029830772 scopus 로고    scopus 로고
    • Three members of a novel small gene family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity also encode a thioredoxin-like domain
    • Guttierez-Marcos J.F., Roberts M.A., Campbell E.I., Wray J.L. Three members of a novel small gene family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity also encode a thioredoxin-like domain. Proc. Natl. Acad. Sci. 93:1996;13377-13382.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 13377-13382
    • Guttierez-Marcos, J.F.1    Roberts, M.A.2    Campbell, E.I.3    Wray, J.L.4
  • 7
    • 0030467396 scopus 로고    scopus 로고
    • The cDNA sequence encoding bovine SP-22, a new defence system against reactive oxygen species in mitochondria
    • Hiroi T., Watabe S., Takimoto K., Yago N., Yamamoto Y., Takahashi S.Y. The cDNA sequence encoding bovine SP-22, a new defence system against reactive oxygen species in mitochondria. DNA Seq. 6:1996;239-242.
    • (1996) DNA Seq. , vol.6 , pp. 239-242
    • Hiroi, T.1    Watabe, S.2    Takimoto, K.3    Yago, N.4    Yamamoto, Y.5    Takahashi, S.Y.6
  • 9
    • 0031444519 scopus 로고    scopus 로고
    • Thioredoxin: Structure and function in plant cells
    • Jacquot J.P., Lancelin J.M., Meyer Y. Thioredoxin: structure and function in plant cells. News Phytol. 136:1997;543-570.
    • (1997) News Phytol. , vol.136 , pp. 543-570
    • Jacquot, J.P.1    Lancelin, J.M.2    Meyer, Y.3
  • 11
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular Cyanobacterium synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko T., et al. Sequence analysis of the genome of the unicellular Cyanobacterium synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3:1996;109-136.
    • (1996) DNA Res. , vol.3 , pp. 109-136
    • Kaneko, T.1
  • 12
    • 0023236892 scopus 로고
    • Duplication of CaMV 35S promoter sequences creates a strong enhancer for plant genes
    • Kay R., Chan A., Daly M., McPherson J. Duplication of CaMV 35S promoter sequences creates a strong enhancer for plant genes. Science. 236:1987;1299-1302.
    • (1987) Science , vol.236 , pp. 1299-1302
    • Kay, R.1    Chan, A.2    Daly, M.3    McPherson, J.4
  • 13
    • 0029911006 scopus 로고    scopus 로고
    • Mitochondria of plant leaves contain two thioredoxins. Completion of the thioredoxin profile of higher plants
    • Konrad A., Banze M., Follmann H. Mitochondria of plant leaves contain two thioredoxins. Completion of the thioredoxin profile of higher plants. Plant Physiol. 149:1996;317-321.
    • (1996) Plant Physiol. , vol.149 , pp. 317-321
    • Konrad, A.1    Banze, M.2    Follmann, H.3
  • 14
    • 0031200830 scopus 로고    scopus 로고
    • High-yield expression of pea thioredoxin m and assessment of its efficiency in chloroplast fructose-1,6-bisphosphatase activation
    • Lopez Jaramillo J., Chueca A., Jacquot J.P., Hermoso R., Lazaro J.J., Sahrawy M., Lopez Gorge J. High-yield expression of pea thioredoxin m and assessment of its efficiency in chloroplast fructose-1,6-bisphosphatase activation. Plant Physiol. 114:1997;1169-1175.
    • (1997) Plant Physiol. , vol.114 , pp. 1169-1175
    • Lopez Jaramillo, J.1    Chueca, A.2    Jacquot, J.P.3    Hermoso, R.4    Lazaro, J.J.5    Sahrawy, M.6    Lopez Gorge, J.7
  • 15
    • 0022495947 scopus 로고
    • Further characterisation and amino acid sequences of m type thioredoxins from spinach chloroplasts
    • Maeda K., Tugita A., Dalzoppo D., Vilbois F., Schürmann P. Further characterisation and amino acid sequences of m type thioredoxins from spinach chloroplasts. Eur. J. Biochem. 154:1986;197-203.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 197-203
    • Maeda, K.1    Tugita, A.2    Dalzoppo, D.3    Vilbois, F.4    Schürmann, P.5
  • 16
    • 0002160837 scopus 로고    scopus 로고
    • Gene transfer from organelles to the nucleus: How much, what happens, and why?
    • Martin W., Herrmann R.G. Gene transfer from organelles to the nucleus: How much, what happens, and why? Plant Physiol. 118:1998;9-17.
    • (1998) Plant Physiol. , vol.118 , pp. 9-17
    • Martin, W.1    Herrmann, R.G.2
  • 17
    • 85047689783 scopus 로고
    • 1H, 13C, 15N-NMR resonance assignments of oxidized thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii using new methods based on two-dimensional triple-resonance NMR spectroscopy and computer-assisted backbone assignment
    • Mittard V., Morelle N., Brutscher B., Simorre J.P., Marion D., Stein M., Jacquot J.P., Lirsac P.N., Lancelin J.M. 1H, 13C, 15N-NMR resonance assignments of oxidized thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii using new methods based on two-dimensional triple-resonance NMR spectroscopy and computer-assisted backbone assignment. Eur. J. Biochem. 229:1995;473-485.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 473-485
    • Mittard, V.1    Morelle, N.2    Brutscher, B.3    Simorre, J.P.4    Marion, D.5    Stein, M.6    Jacquot, J.P.7    Lirsac, P.N.8    Lancelin, J.M.9
  • 18
    • 0031026291 scopus 로고    scopus 로고
    • NMR solution structure of oxidized thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii
    • Mittard V., Blackledge M., Stein M., Jacquot J.P., Marion D., Lancelin J.M. NMR solution structure of oxidized thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii. Eur. J. Biochem. 243:1997;374-383.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 374-383
    • Mittard, V.1    Blackledge, M.2    Stein, M.3    Jacquot, J.P.4    Marion, D.5    Lancelin, J.M.6
  • 19
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai K., Kanehisa M. A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics. 14:1992;897-911.
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 20
    • 0033525509 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae
    • Pedrajas J.R., Kosmidou E., Miranda-Vizuete A., Gustafsson J.A., Wright A.P., Spyrou G. Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae. J. Biol. Chem. 274:1999;6366-6373.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6366-6373
    • Pedrajas, J.R.1    Kosmidou, E.2    Miranda-Vizuete, A.3    Gustafsson, J.A.4    Wright, A.P.5    Spyrou, G.6
  • 21
    • 0028773644 scopus 로고
    • The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin
    • Qin J., Clore G.M., Gronenborn A.M. The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure. 2:1994;503-522.
    • (1994) Structure , vol.2 , pp. 503-522
    • Qin, J.1    Clore, G.M.2    Gronenborn, A.M.3
  • 22
    • 0031885601 scopus 로고    scopus 로고
    • A novel thioredoxin-like protein located in the chloroplast is induced by water deficit in Solanum tuberosum L plants
    • Rey P., Pruvot G., Becuwe N., Eymery F., Rumeau D., Peltier G. A novel thioredoxin-like protein located in the chloroplast is induced by water deficit in Solanum tuberosum L plants. Plant J. 13:1998;97-107.
    • (1998) Plant J. , vol.13 , pp. 97-107
    • Rey, P.1    Pruvot, G.2    Becuwe, N.3    Eymery, F.4    Rumeau, D.5    Peltier, G.6
  • 24
    • 0025325932 scopus 로고
    • Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis
    • Russel M., Model P., Holmgren A. Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis. J. Bacteriol. 172:1990;1923-1929.
    • (1990) J. Bacteriol. , vol.172 , pp. 1923-1929
    • Russel, M.1    Model, P.2    Holmgren, A.3
  • 25
    • 0029645581 scopus 로고
    • Crystal structure of thioredoxin-2 from Anabaena
    • Saarinen M., Gleason F.K., Eklund H. Crystal structure of thioredoxin-2 from Anabaena. Structure. 3:1995;1097-1108.
    • (1995) Structure , vol.3 , pp. 1097-1108
    • Saarinen, M.1    Gleason, F.K.2    Eklund, H.3
  • 27
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:1987;406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 28
    • 1842407157 scopus 로고    scopus 로고
    • Kinetics and thioredoxin specificity of thiol modulation of the chloroplast H+-ATPase
    • Schwarz O., Schürmann P., Strotmann H. Kinetics and thioredoxin specificity of thiol modulation of the chloroplast H+-ATPase. J. Biol. Chem. 272:1997;16924-16927.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16924-16927
    • Schwarz, O.1    Schürmann, P.2    Strotmann, H.3
  • 29
    • 0029841432 scopus 로고    scopus 로고
    • Sulfate reduction in higher plants: Molecular evidence for a novel 6′-adenylylphosphosulfate (APS) reductase
    • Selyat A., Murillo M., Leustek T. Sulfate reduction in higher plants: molecular evidence for a novel 6′-adenylylphosphosulfate (APS) reductase. Proc. Natl. Acad. Sci. 93:1996;13383-13388.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 13383-13388
    • Selyat, A.1    Murillo, M.2    Leustek, T.3
  • 30
    • 0032168004 scopus 로고    scopus 로고
    • Protein translocation into and across the chloroplastic envelope membranes
    • Soll J., Tien R. Protein translocation into and across the chloroplastic envelope membranes. Plant Mol. Biol. 38:1998;191-207.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 191-207
    • Soll, J.1    Tien, R.2
  • 32
    • 0029310608 scopus 로고
    • Chlamydomonas reinhardtii thioredoxins: Structure of the genes coding for the chloroplastic m and cytosolic h isoforms, expression in Escherichia coli of the recombinant proteins, purification and biochemical properties
    • Stein M., Jacquot J.P., Jeannette E., Decottignies P., Hodges M., Lancelin J.M., Mittard V., Schmitter J.M., Miginiac-Maslow M. Chlamydomonas reinhardtii thioredoxins: structure of the genes coding for the chloroplastic m and cytosolic h isoforms, expression in Escherichia coli of the recombinant proteins, purification and biochemical properties. Plant Mol. Biol. 28:1995;487-503.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 487-503
    • Stein, M.1    Jacquot, J.P.2    Jeannette, E.3    Decottignies, P.4    Hodges, M.5    Lancelin, J.M.6    Mittard, V.7    Schmitter, J.M.8    Miginiac-Maslow, M.9
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • Von Heijne G., Steppuhn J., Herrmann R.G. Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 180:1989;535-545.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 36
    • 0026815922 scopus 로고
    • Nucleotide sequence of cDNAs encoding the entire precursor polypeptide for thioredoxin m from spinach chloroplasts
    • Wedel N., Clausmeyer S., Herrmann R.G., Gardet-Salvi L., Schürmann P. Nucleotide sequence of cDNAs encoding the entire precursor polypeptide for thioredoxin m from spinach chloroplasts. Plant Mol. Biol. 18:1992;527-533.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 527-533
    • Wedel, N.1    Clausmeyer, S.2    Herrmann, R.G.3    Gardet-Salvi, L.4    Schürmann, P.5


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